Evidence map›Paper›PMID 20392690›Full record

ArticleThe Journal of biological chemistry2010

Compensations for diminished terminal oxidase activity in Escherichia coli: cytochrome bd-II-mediated respiration and glutamate metabolism.

Mark Shepherd, Guido Sanguinetti, Gregory M Cook, Robert K Poole

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Mechanistic and structural diversity between cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Development of Resistance inAntibiotics (Basel, Switzerland) · 2020
    Article
  9. Review
  10. Article
  11. TheAIMS microbiology · 2017
    Article
  12. Article
  13. Oxygen as Acceptor.EcoSal Plus · 2015
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. The cytochrome bd respiratory oxygen reductases.Biochimica et biophysica acta · 2011
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Mark ShepherdDepartment of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, United Kingdom.
Guido Sanguinetti
Gregory M Cook
Robert K Poole
University of Sheffield · GBUniversity of Edinburgh · GBUniversity of Otago · NZ

Funding

Biotechnology and Biological Sciences Research Council BB/C514174/1Biotechnology and Biological Sciences Research Council BB/F003463/1
6 · The paper itself

Abstract

Escherichia coli possesses cytochrome bo' (CyoABCDE), cytochrome bd-I (CydAB), and cytochrome bd-II (AppBC) quinol oxidases, all of which can catalyze the terminal step in the aerobic respiratory chain, the reduction of oxygen by ubiquinol. Although CydAB has a role in the generation of DeltapH, AppBC has been proposed to alleviate the accumulation of electrons in the quinone pool during respiratory stress via electroneutral ubiquinol oxidation. A cydB mutant strain exhibited lower respiration rates while maintaining a wild type growth rate. Transcriptomic analysis revealed a dramatic up-regulation of AppBC in the cydB strain, accompanied by the induction of genes involved in glutamate/gamma-aminobutyric acid (GABA) antiport, the GABA shunt, the glyoxylate shunt, respiration (including appBC), motility, and osmotic stress. Transcription factor modeling suggests that the underpinning regulation is largely controlled by H-NS, GadX, FlhDC, and AppY. The transcriptional adaptations imply that cydB cells contribute to the proton motive force via consumption of intracellular protons and glutamate/GABA antiport. Indeed, supplementation of culture medium with l-glutamate stimulates growth in a cydB strain. Phenotype analyses of the cydB strain confirm decreased motility and elevated acid resistance and also an elevated cytochrome d spectroscopic signal in cells grown at low pH. We propose a mechanism via which E. coli can compensate for the loss of cytochrome bd-I activity; cytochrome bd-II-mediated quinol oxidation prevents the accumulation of NADH, whereas GABA synthesis/antiport maintains the proton motive force for ATP production.

Indexed as

Oxygen ConsumptionCell MovementCell RespirationCytochrome d GroupCytochromes bElectrodesEscherichia coliGene Expression Regulation, BacterialGlutamatesGlutamic AcidHydrogen-Ion ConcentrationKineticsModels, StatisticalOxygenSpectrophotometryCytochrome d GroupCytochromes bGlutamatesGlutamic AcidOxygen

Identifiers

PMID20392690
PMCPMC2881772
OpenAlexW2027256175

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.